STAMBPL1 CRISPR Activation Plasmid (h): sc-405119-ACT

STAMBPL1 (STAM binding protein-like 1) encodes a JAMM-family zinc metalloprotease deubiquitinase that participates in endosomal sorting and ubiquitin-dependent regulation of membrane protein turnover. By modulating deubiquitination events linked to ESCRT-associated trafficking, STAMBPL1 influences receptor internalization, signal attenuation, and proteostasis across endolysosomal pathways. Its activity connects ubiquitin signaling to cellular responses such as growth factor receptor routing, inflammatory signaling dynamics, and stress-adaptive remodeling of the endomembrane system. Dysregulated ubiquitin editing and endosomal trafficking are broadly implicated in cancer biology, neurodegeneration, and immune dysfunction, making STAMBPL1 a relevant node for mechanistic studies of these processes.

STAMBPL1 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous STAMBPL1 expression without altering the underlying DNA sequence.

STAMBPL1 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the STAMBPL1 locus in human cell lines. The system is built around a catalytically inactive Cas9 (dCas9) carrying two inactivating mutations (D10A and N863A) that eliminate nuclease activity while preserving DNA binding. This dCas9 is fused to VP64, a potent transcriptional activator, and is co-expressed with a blasticidin resistance gene for selection. The second plasmid encodes the MS2-p65-HSF1 fusion protein, a secondary activator complex that works in concert with dCas9-VP64, alongside a hygromycin resistance gene. The third plasmid encodes a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers that recruit the MS2-p65-HSF1 complex to the activation site, accompanied by a puromycin resistance gene. The three plasmids are delivered at a 1:1:1 mass ratio for balanced expression of all system components.

Once assembled at the target locus, the SAM complex binds within approximately 200 bp upstream of the STAMBPL1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous STAMBPL1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native STAMBPL1 locus and enabling the study of STAMBPL1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of STAMBPL1 pathway restoration in tumor cells with silenced or reduced STAMBPL1 expression.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.